Characterization of polyanionic collagen prepared by selective hydrolysis of asparagine and glutamine carboxyamide side chains.

Acellular polyanionic collagen materials intended for biomaterial and tissue engineering uses were prepared by the selective and controlled hydrolysis of carboxyamides from asparagine and glutamine residues of type I collagen present in pericardium, tendon, and intestinal submucosa, all from bovine origin. The increase in carboxyl groups was from 26 +/- 14 (12 h of hydrolysis) to 134 +/- 12 (144 h of hydrolysis). Although collagen triple helix structure of polyanionic materials was preserved in all cases, a decrease in thermal stability and a gradual loss in the ability of collagen molecules to form fibrils were detected with increasing carboxyl content, probably as a result of changes in the pattern of electrostatic interaction. The resulting materials were basically acellular polyanionic collagen matrixes associated with an elastin content dependent on the time of hydrolysis. The results showed that the procedure described in this work may be a useful process for preparation of collagen biomaterials with variable physicochemical properties and macromolecular arrangement with respect to fibril formation and with potential use in tissue engineering.